cbiM1 is produced via recombinant expression in E. coli, with an N-terminal His-tag for purification and detection. Key parameters include:
The protein is commercially available in lyophilized or liquid forms, with applications in structural studies, enzymatic assays, and ELISA-based research .
| Component | Role | Interaction |
|---|---|---|
| cbiM (cbiM1) | Substrate capture (cobalt) | Binds CbiQO, stimulates ATPase |
| CbiQ (EcfT) | Membrane scaffold | Couples cbiM and CbiO |
| CbiO (EcfA) | ATP-binding/hydrolysis component | Regulates conformational changes |
The transport mechanism involves coordinated rotation of CbiQ and CbiM, driven by ATP binding and hydrolysis .
cbiM1 is integral to studying cobalt-dependent metabolic pathways and host-microbe interactions:
Methanogenesis: M. labreanum uses cobalt-containing enzymes (e.g., methyl-coenzyme M reductase) for methane production. cbiM1 may enable cobalt acquisition, supporting this process .
Host Adaptation: Host-associated Methanocorpusculum species (e.g., M. vombati, M. petauri) rely on nutrient uptake systems like ECF transporters for survival in symbiotic niches .
M. labreanum and related species exhibit distinct genetic adaptations:
These differences highlight cbiM1’s potential role in host-specific nutrient acquisition .
KEGG: mla:Mlab_0380
STRING: 410358.Mlab_0380